![]() ![]() Parallel selections were performed with a library having diversity spread onto a greater area, including more peripherally located residues. The library was screened, using phage display, against a panel of different haptens, yielding diverse and highly specific binders to four of the antigens. Altogether a library with diversity limited to a part of the binding site likely to interact with haptens (Figure 1). In addition, length variation was introduced in H2 as longer versions of this loop have been shown to correlate with increased hapten binding. CDR元 was allowed to carry a more complex type of diversity. In five of the six CDR-loops, diversity carrying residues were rationally selected based on a model structure of FITC8 and on known antibody structure-function relationships, resulting in variation of 11 centrally located, cavity-lining residues. This scFv, like other hapten binders, display a characteristic cavity in its paratope into which the hapten binds. The hapten specific scFv, FITC8, was used as a scaffold for library construction. Based on these considerations we have designed (Persson et al., 2006) a focused single chain antibody fragment (scFv) repertoire biased for haptens, designated the cavity library. ![]() Such topography is strongly correlated to the size of the antigen to which the antibody interacts. The topography of an antigen-binding site is determined by the length and sequence composition of the CDR loops as well as by the number and positioning of the antigen contact residues. ![]()
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